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. Author manuscript; available in PMC: 2017 Jul 19.
Published in final edited form as: J Med Chem. 2008 Dec 25;51(24):7737–7743. doi: 10.1021/jm800765e

Figure 3.

Figure 3

(A) Superposition of urea-based inhibitors in the active-site of rhGCPII. The rhGCPII–inhibitor complexes were superimposed on corresponding Cα-atoms. The inhibitors are shown in stick representation and protein residues are shown as lines. Note invariant positioning of the P1′ glutamate contrasting with inhibitor conformational variability in the S1 pocket. (B) Hydrogen-bonding network in the S1 site of GCPII. Hydrogen bonding interactions (indicated with dashed lines) and distances (in Ångstroms) between 1 bound in the active site and S1 residues of GCPII. The zinc ions, chloride anion, and water molecules located in the active site are shown as blue, yellow and red spheres, respectively. The protein and inhibitor atoms are colored red (oxygen), blue (nitrogen), yellow (sulfur), violet (iodine), cyan (fluorine), gray (carbons).